Synthesis, purification and kinetic properties of fluorescein-labelled penicillins

Biochem J. 1994 May 15;300 ( Pt 1)(Pt 1):141-5. doi: 10.1042/bj3000141.

Abstract

The synthesis and properties of six fluorescein-labelled penicillins are reported. The two isomers of fluoresceyl-glycyl-6-amino-penicillanic acid are probably the best compounds to use for detection of all the penicillin-binding proteins (PBPs) present in a bacterial membrane preparation. However, the derivatives of ampicillin were much more efficient against Enterobacter aerogenes PBP3. The two isomers obtained when a commercial mixture of the two isomers of carboxyfluorescein was used most often exhibited similar properties, but the Streptomyces R61 extracellular DD-peptidase was only efficiently acylated by the 5'-carboxyfluorescein derivative of glycyl-6-aminopenicillanic acid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Carrier Proteins / metabolism
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Fluorescein
  • Fluoresceins / chemistry*
  • Hexosyltransferases*
  • Magnetic Resonance Spectroscopy
  • Muramoylpentapeptide Carboxypeptidase / metabolism
  • Penicillin-Binding Proteins
  • Penicillins / biosynthesis*
  • Penicillins / isolation & purification
  • Penicillins / metabolism
  • Peptidyl Transferases*

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Fluoresceins
  • Penicillin-Binding Proteins
  • Penicillins
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • Fluorescein